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| Description | GLR-19 (CAS: 1225014-05-0) is a 19-residue cationic antiviral peptide designed by database-guided design, sequence GLRRLLGRLLRRLGRLLLR. Molecular formula C102H194N40O20, MW 2300.89 Da. GLR-19 was derived from GLK-19 (GLKKLLGKLLKKLGKLLLK) by replacing all lysines (Lys/K) with arginines (Arg/R) to improve protease stability and antiviral activity. GLR-19 has an EC50 of 4.4 uM against HIV-1 and antiviral activity against HSV-2, with some antibacterial activity (MIC 120 uM). GLR-19 adopts an alpha-helical amphipathic structure; the guanidinium groups of Arg residues form stronger electrostatic and hydrogen-bond interactions with viral envelopes and cell membrane phospholipids. GLR-19 is a tool for studying cationic antiviral peptide design, HIV membrane fusion inhibition, and Arg-substitution strategies. |
| Structure type | Linear 19-mer (Gly-Leu-Arg repeat designed cationic antiviral alpha-helical peptide) |
| Solubility | Readily soluble in water, dilute acetic acid |
| Storage | Powder -20C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| GLR-19 (de novo-designed anti-HIV arginine-rich peptide) | GLR-19; GLK-19 Arg analog | Antiviral, anti-HIV, anti-HSV-2, antibacterial, de novo-designed peptide, cationic amphipathic | Linear 19-aa de novo-designed cationic amphipathic α-helical peptide composed solely of Gly(3), Leu(9), and Arg(7); net charge +7 (no acidic residues); derived from GLK-19 by Lys→Arg substitution; periodic sequence repeats (GLRRLL-GRLLRRL-GRLLLR) form amphipathic helix with Arg-rich hydrophilic face and Leu-rich hydrophobic face | C₁₀₂H₁₉₄N₄₀O₂₀ (free acid) | 2299.54 | 2300.93 | Free peptide (typically supplied as TFA or acetate salt after RP purification) | 19 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-GLR19-01 | White powder | Store at -20°C, sealed, desiccated, protected from light (stable 3 years). No Cys/Met/Trp-excellent chemical stability, no inert gas required. Aliquot to avoid repeated freeze-thaw. | 2–8°C, sealed and desiccated (long-term); stable for shipping at ambient. Working aliquots at -80°C for up to 1 year. | Highly cationic (7 Arg, no acidic residues, net +7) with a long Leu-rich hydrophobic surface, but the dense positive charge confers good water solubility (≥2–5 mg/mL in water/aqueous buffers); no organic co-solvent needed. Contains no Cys (no disulfide), no Met (no oxidation), no Trp (no photo-oxidation)-among the most chemically stable peptides in the series. The amphipathic helix may self-aggregate in aqueous solution; prepare working solutions fresh. | solid stable for 3 years at -20°C, sealed and desiccated. Excellent chemical stability; low hygroscopicity. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-GLR19-01 | A de novo-designed 19-aa Gly/Leu/Arg-rich cationic amphipathic peptide, engineered from GLK-19 by Lys→Arg substitution, with anti-HIV-1, anti-HSV-2, and antibacterial activity. | GLR-19 is a 19-residue amphipathic α-helical peptide designed by database-guided analysis of antimicrobial peptides. The parent GLK-19 scaffold was built using only Gly, Leu, and Lys; replacing all Lys with Arg yielded GLR-19 with significantly enhanced anti-HIV-1 activity-the guanidinium group of Arg provides stronger membrane interaction and viral envelope disruption than the ammonium group of Lys. GLR-19 inhibits both HIV-1 and HSV-2 while retaining antibacterial activity against E. coli. Its mechanism involves electrostatic recruitment to negatively charged viral envelopes/bacterial membranes via Arg residues, followed by insertion of the Leu-rich hydrophobic helix into the lipid bilayer, causing membrane disruption and blocking viral entry. This peptide is a valuable tool for studying de novo-designed antiviral peptides and membrane-virus interactions. | Antiviral peptide design, HIV-1/HSV-2 microbicides, de novo peptide engineering, membrane-virus interactions, AMP database-driven design | Enveloped virus membranes / viral entry stages (HIV-1, HSV-2); anionic lipid bilayer disruption; arginine-mediated membrane/cell surface binding |
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